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Purification of poly-histidine-tagged proteins.

Sinéad T ST Loughran and Dermot D Walls

Methods Mol Biol (2011) PMID 20978973

His-tagging is the most widespread and versatile strategy used to purify recombinant proteins for biochemical and structural studies. Recombinant DNA methods are first used to engineer the addition of a short tract of poly-histidine tag (His-tag) to the N terminus or C terminus of a target protein. The His-tag is then exploited to enable purification of the "tagged" protein by immobilised metal affinity chromatography (IMAC). Here, we describe efficient procedures for the isolation of highly purified His-tagged target proteins from an Escherichia coli host using IMAC.

DOI: 10.1007/978-1-60761-913-0_17
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